Popular Articles
- Crystal structure of CO-bound cytochrome c oxidase determined by serial femtosecond X-ray crystallography at room temperature
- NSF awards $22.5 million to capture biology at the atomic level using X-ray lasers
- BioXFEL Research Support Call for Proposals
- Frankuchen Award : ACA 2019
- UWM researchers create first 3D movie of virus in action
Archived Articles
- Details
- Thursday, 10 August 2017
BioXFEL scientist Vadim Cherezov and his colleagues released a new publication to CellPress:
X-ray free electron lasers (XFELs) have the potential to revolutionize macromolecular structural biology due to the unique combination of spatial coherence, extreme peak brilliance, and short duration of X-ray pulses. A recently emerged serial femtosecond (fs) crystallography (SFX) approach using XFEL radiation overcomes some of the biggest hurdles of traditional crystallography related to radiation damage through the diffraction-before-destruction principle.
Intense fs XFEL pulses enable high-resolution room-temperature structure determination of difficult-to-crystallize biological macromolecules, while simultaneously opening a new era of time-resolved structural studies. Here, we review the latest developments in instrumentation, sample delivery, data analysis, crystallization methods, and applications of SFX to important biological questions, and conclude with brief insights into the bright future of structural biology using XFELs.